Functions of the nuclear ubiquitin proteasome system regulated by N-myristoylation

2014 Fiscal Year Final Research Report

• Project/Area Number: 25840039
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Functional biochemistry
• Research Institution: Yokohama City University
• Principal Investigator: KIMURA Ayuko 横浜市立大学, 生命医科学研究科, 特任助教 (50553616)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: ユビキチン / ミリストイル化 / プロテアソーム / プロテオミクス / Rpt2 / 翻訳後修飾 / 核 / 細胞内局在

Outline of Final Research Achievements

N-Myristoylation is expected to control the compartmentalized proteolysis within the cells via dynamic regulation of the nucleo-cytoplasmic localization of proteasome. To obtain the comprehensive view on the substrates and physiological functions of this control system, ubiquitin proteome analysis was performed using the yeast strains with or without mutation on the N-myristoylation site of proteasome subunit Rpt2. The ubiquitination levels of the two heat shock proteins involved in the nuclear transport of proteins as well as those of some possible nucleo-cytoplasmic proteins, which are involved in the stress response and metabolism, were significantly upregulated in the mutant strains. These results indicate that the N-myristoylation of proteasome is implicated in the stress response by controlled proteolysis of a part of cytoplasmic proteins within the nucleus.

Free Research Field

プロテオミクス、分子生物学